Hormones, lipid soluble vitamins and the like play an important role in homoestatic maintenance, energy metabolism, differentiation, and growth of organisms. Transcription control factors are receptors for such hormones and reside in nuclei where they bind with particular sites of chromatin DNA to control the transcription reaction of genes. In most cases, when ligands such as a hormone are not bound with a receptor, transcription is repressed from occurring. Once a ligand, such as a hormone, binds to a receptor, the transcription is activated through a change in the chromatin structure. It has been reported that many factors called co-activators and co-repressors work by forming complexes along the pathway leading from nuclear receptors to the transcription apparatus (transcriptor). When a co-repressor complex containing a histone deacetylase binds with a receptor that is itself not bound to a ligand, gene expression is repressed. On the other hand, when the receptor structure is changed upon binding by a ligand, the co-repressor complex is released and, instead, a co-activator complex containing a histone acetylase is recruited. Mention is made, as an instance of such a co-activator, of Skip (i.e. Ski interacting protein, and also called N-CoA62), which can directly bind to several types of nuclear receptors (e.g. vitamin 3 receptor, retinoic acid receptor, estrogen receptor and glucomulticoid receptor) to strengthen the gene expression mediated by these nuclear receptors (Baudino, T. A., Kraichely, D. M., Jefcoat, S. C., Jr., Winchester, S. K., Partridge, N. C., and MacDonaldo, P. N. (1998) J. Biol. Chem. 273(26), 16434-41, MacDonald, P. N., Baudio, T. A., Tokumaru, H., Dowd, D. R., and Zhang, C. (2001) Steroids 66(3-5), 171-6).